Abstract
In human health and disease the choreographed actions of a wide armory of transcription factors govern the regulated expression of coding and nonprotein coding genes. These actions are central to human health and are evidently aberrant in cancer. Central components of regulated gene expression are a variety of epigenetic mechanisms that include histone modifications. The post-translational modifications of histones are widespread and diverse, and appear to be spatial-temporally regulated in a highly intricate manner. The true functional consequences of these patterns of regulation are still emerging. Correlative evidence supports the idea that these patterns are distorted in malignancy on both a genome-wide and a discrete gene loci level. These patterns of distortion also often reflect the altered expression of the enzymes that control these histone states. Similarly gene expression patterns also appear to reflect a correlation with altered histone modifications at both the candidate loci and genome-wide level. Clarity is emerging in resolving these relationships between histone modification status and gene expression patterns. For example, altered transcription factor interactions with the key co-activator and co-repressors, which in turn marshal many of the histone-modifying enzymes, may distort regulation of histone modifications at specific gene loci. In turn these aberrant transcriptional processes can trigger other altered epigenetic events such as DNA methylation and underline the aberrant and specific gene expression patterns in cancer. Considered in this manner, altered expression and recruitment of histone-modifying enzymes may underline the distortion to transcriptional responsiveness observed in malignancy. Insight from understanding these processes addresses the challenge of targeted epigenetic therapies in cancer.
Keywords
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
Chromatin-modifying enzymes: The nomenclature for enzymes involved in protein methylation, demethylation, and acetylation has recently been rationalized (Allis CD et al (2007) New nomenclature for chromatin-modifying enzymes. Cell 131:633–636). In this review, we use the new nomenclature for lysine methyltransferases (KMT), lysine demethylases (KDM), and lysine acetyltransferases (KAT). Histone deacetylases (HDACs) have retained their original nomenclature. To maintain a link between the new nomenclature and the literature, we use both the new designation and the original published designation(s), e.g., KDM5A/JARID1A/RBP2.
Histone modifications: We use the Brno nomenclature for histone modifications (Turner BM (2005) Reading signals on the nucleosome with a new nomenclature for modified histones. Nat Struct Mol Biol 12:110–112). For example, histone H3 tri-methylated at lysine 4 is shown as H3K4me3.
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Abbreviations
- AR:
-
Androgen receptor
- ChIP:
-
Chromatin immunoprecipitation
- CoA:
-
Co-activator complex
- E2 :
-
Estradiol
- ERα:
-
Estrogen receptor alpha
- ES:
-
Embryonic stem cell
- HDAC:
-
Histone deacetylase
- JMJD:
-
Jumonji domain containing protein
- JARID:
-
Jumonji AT-rich interactive domain
- KAT:
-
Lysine acetyltransferase
- KDM:
-
Lysine demethylase
- KMT:
-
Lysine methyltransferase
- LSD1:
-
Lysine-specific demethylase 1
- NCOR:
-
Nuclear co-repressor
- NR:
-
Nuclear receptor
- PSA:
-
Prostate-specific antigen
- SET:
-
Su(var), enhancer of zeste and trithorax
- TF:
-
Transcription factor
- TSA:
-
Trichostatin A
- TSS:
-
Transcription start site
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Campbell, M.J., Turner, B.M. (2013). Altered Histone Modifications in Cancer. In: Karpf, A. (eds) Epigenetic Alterations in Oncogenesis. Advances in Experimental Medicine and Biology, vol 754. Springer, New York, NY. https://doi.org/10.1007/978-1-4419-9967-2_4
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